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J Biol Chem, Vol. 273, Issue 19, 11521-11526, May 8, 1998
From the Department of Biochemistry, University of Vermont College
of Medicine, Burlington, Vermont 05405-0068
Human factor Xa specifically cleaves the
anticoagulant protein S within the thrombin-sensitive domain.
Amino-terminal amino acid sequencing of the heavy chain cleavage
product indicates cleavage of protein S by factor Xa at
Arg60, a site that is distinct from those utilized by
Human Protein S Cleavage and Inactivation by Coagulation
Factor Xa
-thrombin. Cleavage by factor Xa is unaffected by the presence of
hirudin and is completely blocked by tick-anticoagulant-peptide and
D-Glu-Gly-Arg-chloromethyl ketone, the latter two being
specific inhibitors of factor Xa. The cleavage requires the presence of
phospholipid and Ca2+, and is markedly inhibited by the
presence of factor Va. Factor Xa-cleaved protein S no longer possesses
its activated protein C-dependent or -independent
anticoagulant activity, as measured in a factor VIII-based activated
partial thromboplastin time clot assay. The apparent binding constant
for protein S binding to phospholipid (Kd 
4 nM ± 1.0) is unaffected by factor Xa or thrombin cleavage,
suggesting that the loss of anticoagulant activity resulting from
cleavage is not primarily due to the loss of membrane binding ability.
Cleavage and inactivation of protein S by factor Xa may be an
additional way in which factor Xa exerts its procoagulant effect, after
the initial stages of clot formation.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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